Evidence map›Paper›PMID 9348534›Full record

ArticleMolecular biology of the cell1997

Segregation of two spectrin isoforms: polarized membrane-binding sites direct polarized membrane skeleton assembly.

R R Dubreuil, P B Maddux, T A Grushko, G R MacVicar

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. The assembly and maintenance of epithelial junctions in C. elegans.Frontiers in bioscience (Landmark edition) · 2009
    Review
  8. Article
  9. Mating induces an immune response and developmental switch in the Drosophila oviduct.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Drosophila alpha- and beta-spectrin mutations disrupt presynaptic neurotransmitter release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

R R DubreuilDepartment of Pharmacological and Physiological Sciences, University of Chicago, Illinois 60637, USA.
P B Maddux
T A Grushko
G R MacVicar
University of Chicago · US

Funding

GENETIC STUDIES OF THE MEMBRANE SKELETONR01GM049301 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI DUBREUIL, RONALD R · 1995 to 2004
$1.1M
NIGMS NIH HHS GM-49301NIGMS NIH HHS R01 GM049301
6 · The paper itself

Abstract

Spectrin isoforms are often segregated within specialized plasma membrane subdomains where they are thought to contribute to the development of cell surface polarity. It was previously shown that ankyrin and beta spectrin are recruited to sites of cell-cell contact in Drosophila S2 cells expressing the homophilic adhesion molecule neuroglian. Here, we show that neuroglian has no apparent effect on a second spectrin isoform (alpha beta H), which is constitutively associated with the plasma membrane in S2 cells. Another membrane marker, the Na,K-ATPase, codistributes with ankyrin and alpha beta spectrin at sites of neuroglian-mediated contact. The distributions of these markers in epithelial cells in vivo are consistent with the order of events observed in S2 cells. Neuroglian, ankyrin, alpha beta spectrin, and the Na,K-ATPase colocalize at the lateral domain of salivary gland cells. In contrast, alpha beta H spectrin is sorted to the apical domain of salivary gland and somatic follicle cells. Thus, the two spectrin isoforms respond independently to positional cues at the cell surface: in one case an apically sorted receptor and in the other case a locally activated cell-cell adhesion molecule. The results support a model in which the membrane skeleton behaves as a transducer of positional information within cells.

Indexed as

AnimalsAnkyrinsBinding SitesCell Adhesion Molecules, NeuronalCell LineCell MembraneCytoskeletonDrosophilaDrosophila ProteinsEpithelial CellsHumansIsomerismOocytesSalivary GlandsSodium-Potassium-Exchanging ATPaseSpectrinAnkyrinsCell Adhesion Molecules, NeuronalDrosophila ProteinsNrg protein, DrosophilaSodium-Potassium-Exchanging ATPaseSpectrin

Identifiers

PMID9348534
PMCPMC25644
OpenAlexW2114330628

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.